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Article: Endoglucanase S, a novel endocellulase exhibiting exoglucanase activity from a newly isolated Streptomyces sp. LX

TitleEndoglucanase S, a novel endocellulase exhibiting exoglucanase activity from a newly isolated Streptomyces sp. LX
Authors
Issue Date1998
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JAM
Citation
Journal Of Applied Microbiology, 1998, v. 85 n. 2, p. 347-356 How to Cite?
AbstractA novel endocellulase, designated as endoglucanase S, was purified to homogeneity from culture supernatant fluids of the newly isolated Streptomyces sp. LX, and shown not to be identical with previously described endo-β-1,4-glucanases. Both endo- and exo-cellulase activities were found to reside on a monomeric protein of 48 kDa. Its temperature optimum is 50 °C, and it was stable at 60 °C. The optimum pH is 5.5, and it has a broad pH stability from pH 3.0-7.0. The action of the enzyme on carboxymethylcellulose (CMC) suggested that the enzyme behaved as endoglucanase, whereas it was also active on crystalline cellulose with cellodextrin as end-product. Fragmentation of filter paper revealed that the degree of polymerization of residual cellulose decreased with time but only 5.2% of filter paper was converted into soluble carbohydrate.
Persistent Identifierhttp://hdl.handle.net/10722/68465
ISSN
2023 Impact Factor: 3.2
2023 SCImago Journal Rankings: 0.764
References

 

DC FieldValueLanguage
dc.contributor.authorLi, Xen_HK
dc.contributor.authorLin, Wen_HK
dc.contributor.authorGao, Pen_HK
dc.contributor.authorChen, Fen_HK
dc.date.accessioned2010-09-06T06:04:51Z-
dc.date.available2010-09-06T06:04:51Z-
dc.date.issued1998en_HK
dc.identifier.citationJournal Of Applied Microbiology, 1998, v. 85 n. 2, p. 347-356en_HK
dc.identifier.issn1364-5072en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68465-
dc.description.abstractA novel endocellulase, designated as endoglucanase S, was purified to homogeneity from culture supernatant fluids of the newly isolated Streptomyces sp. LX, and shown not to be identical with previously described endo-β-1,4-glucanases. Both endo- and exo-cellulase activities were found to reside on a monomeric protein of 48 kDa. Its temperature optimum is 50 °C, and it was stable at 60 °C. The optimum pH is 5.5, and it has a broad pH stability from pH 3.0-7.0. The action of the enzyme on carboxymethylcellulose (CMC) suggested that the enzyme behaved as endoglucanase, whereas it was also active on crystalline cellulose with cellodextrin as end-product. Fragmentation of filter paper revealed that the degree of polymerization of residual cellulose decreased with time but only 5.2% of filter paper was converted into soluble carbohydrate.en_HK
dc.languageengen_HK
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JAMen_HK
dc.relation.ispartofJournal of Applied Microbiologyen_HK
dc.rightsJournal of Applied Microbiology. Copyright © Blackwell Publishing Ltd.en_HK
dc.titleEndoglucanase S, a novel endocellulase exhibiting exoglucanase activity from a newly isolated Streptomyces sp. LXen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1364-5072&volume=85&spage=347&epage=356&date=1998&atitle=Endoglucanase+S,+a+novel+endocellulase+exhibiting+exoglucanase+activity+from+a+newly+isolated+Streptomyces+sp.+LXen_HK
dc.identifier.emailChen, F: sfchen@hku.hken_HK
dc.identifier.authorityChen, F=rp00672en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1046/j.1365-2672.1998.00518.xen_HK
dc.identifier.scopuseid_2-s2.0-0031708537en_HK
dc.identifier.hkuros45461en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031708537&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume85en_HK
dc.identifier.issue2en_HK
dc.identifier.spage347en_HK
dc.identifier.epage356en_HK
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLi, X=7501701424en_HK
dc.identifier.scopusauthoridLin, W=35080673000en_HK
dc.identifier.scopusauthoridGao, P=7201740410en_HK
dc.identifier.scopusauthoridChen, F=7404907980en_HK
dc.identifier.issnl1364-5072-

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